P12281 (MOEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Molybdopterin molybdenumtransferase
Short name=MPT Mo-transferase
EC=2.10.1.1

Gene names

Name:	moeA
Synonyms:	bisB, chlE, narE
Ordered Locus Names:	b0827, JW0811

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Ref.6
Catalytic activity	Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.
Cofactor	Binds 1 magnesium ion per subunit. Ref.7
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Subunit structure	Homodimer. Ref.7 Ref.8
Sequence similarities	Belongs to the moeA family.

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Ligand	Magnesium Metal-binding Molybdenum
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mobA	P32173	3	EBI-554393,EBI-1133881

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 411

411

Molybdopterin molybdenumtransferase

PRO_0000170989

Secondary structure

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411

Helix Strand Turn

Details...

Helix

10 – 20

11

Beta strand

27 – 31

5

Helix

32 – 34

3

Beta strand

39 – 42

4

Beta strand

50 – 53

4

Beta strand

55 – 63

9

Helix

65 – 68

4

Beta strand

76 – 80

5

Beta strand

82 – 84

3

Beta strand

95 – 98

4

Beta strand

110 – 113

4

Helix

114 – 116

3

Beta strand

117 – 120

4

Beta strand

123 – 126

4

Turn

132 – 135

4

Beta strand

141 – 143

3

Beta strand

148 – 150

3

Turn

158 – 160

3

Helix

161 – 165

5

Turn

166 – 168

3

Beta strand

171 – 175

5

Beta strand

179 – 185

7

Helix

205 – 215

11

Beta strand

219 – 226

8

Helix

230 – 242

13

Beta strand

245 – 249

5

Beta strand

251 – 253

3

Beta strand

255 – 257

3

Helix

260 – 268

9

Beta strand

269 – 280

12

Beta strand

283 – 288

6

Beta strand

290 – 296

7

Helix

301 – 310

10

Helix

312 – 319

8

Beta strand

331 – 337

7

Beta strand

345 – 355

11

Beta strand

361 – 365

5

Helix

376 – 379

4

Beta strand

382 – 386

5

Beta strand

398 – 403

6

Sequences

	Sequence		Length	Mass (Da)
	P12281 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 6DBBC2B4191F5951	FASTA	411	44,067
	10 20 30 40 50 60 MEFTTGLMSL DTALNEMLSR VTPLTAQETL PLVQCFGRIL ASDVVSPLDV PGFDNSAMDG 70 80 90 100 110 120 YAVRLADIAS GQPLPVAGKS FAGQPYHGEW PAGTCIRIMT GAPVPEGCEA VVMQEQTEQM 130 140 150 160 170 180 DNGVRFTAEV RSGQNIRRRG EDISAGAVVF PAGTRLTTAE LPVIASLGIA EVPVIRKVRV 190 200 210 220 230 240 ALFSTGDELQ LPGQPLGDGQ IYDTNRLAVH LMLEQLGCEV INLGIIRDDP HALRAAFIEA 250 260 270 280 290 300 DSQADVVISS GGVSVGEADY TKTILEELGE IAFWKLAIKP GKPFAFGKLS NSWFCGLPGN 310 320 330 340 350 360 PVSATLTFYQ LVQPLLAKLS GNTASGLPAR QRVRTASRLK KTPGRLDFQR GVLQRNADGE 370 380 390 400 410 LEVTTTGHQG SHIFSSFSLG NCFIVLERDR GNVEVGEWVE VEPFNALFGG L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis." Nohno T., Kasai Y., Saito T. J. Bacteriol. 170:4097-4102(1988) [PubMed: 3045084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli." Hasona A., Ray R.M., Shanmugam K.T. J. Bacteriol. 180:1466-1472(1998) [PubMed: 9515915] [Abstract] Cited for: CHARACTERIZATION.
[6]	"In vitro molybdenum ligation to molybdopterin using purified components." Nichols J.D., Rajagopalan K.V. J. Biol. Chem. 280:7817-7822(2005) [PubMed: 15632135] [Abstract] Cited for: FUNCTION AS MPT--MO LIGASE.
[7]	"The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway." Schrag J.D., Huang W., Sivaraman J., Smith C., Plamondon J., Larocque R., Matte A., Cygler M. J. Mol. Biol. 310:419-431(2001) [PubMed: 11428898] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION, SUBUNIT, COFACTOR.
[8]	"The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin." Xiang S., Nichols J., Rajagopalan K.V., Schindelin H. Structure 9:299-310(2001) [PubMed: 11525167] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M21151 Genomic DNA. Translation: AAA23579.1.
U00096 Genomic DNA. Translation: AAC73914.1.
AP009048 Genomic DNA. Translation: BAA35515.1.

PIR

A32352.

RefSeq

NP_415348.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FC5	X-ray	2.20	A/B	1-411	[»]
1G8L	X-ray	1.95	A/B	1-411	[»]
1G8R	X-ray	2.65	A/B	1-411	[»]
2NQK	X-ray	2.90	A/B	1-411	[»]
2NQM	X-ray	3.00	A/B	1-411	[»]
2NQN	X-ray	2.20	A/B	1-411	[»]
2NQQ	X-ray	2.40	A/B/C/D	1-411	[»]
2NQR	X-ray	2.20	A/B	1-411	[»]
2NQS	X-ray	2.50	A/B	1-411	[»]
2NQU	X-ray	2.70	A/B	1-411	[»]
2NQV	X-ray	2.82	A/B	1-411	[»]
2NRO	X-ray	2.50	A/B	1-411	[»]
2NRP	X-ray	3.00	A/B	1-411	[»]
2NRS	X-ray	2.80	A/B	1-411	[»]

ProteinModelPortal

P12281.

SMR

P12281. Positions 5-408.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10240N.

IntAct

P12281. 10 interactions.

MINT

MINT-1250871.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000620; EBESCP00000000620; EBESCG00000000516.
EBESCT00000017967; EBESCP00000017258; EBESCG00000017023.

GeneID

945454.

GenomeReviews

Gene locus JW0811 in contig AP009048_GR.
Gene locus b0827 in contig U00096_GR.

KEGG

ecj:JW0811.
eco:b0827.

PATRIC

32116857. VBIEscCol129921_0854.

Organism-specific databases

EchoBASE

EB0151.

EcoGene

EG10153. moeA.

Phylogenomic databases

eggNOG

COG0303.

GeneTree

EBGT00050000011591.

HOGENOM

HBG731522.

OMA

VPGFDNA.

PhylomeDB

P12281.

ProtClustDB

PRK10680.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10153-MONOMER.
MetaCyc:EG10153-MONOMER.

Gene expression databases

Genevestigator

P12281.

Family and domain databases

InterPro

IPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd.
[Graphical view]

Gene3D

G3DSA:2.40.340.10. G3DSA:2.40.340.10. 1 hit.
G3DSA:3.40.980.10. MPT_bd. 1 hit.

KO

K03750.

Pfam

PF00994. MoCF_biosynth. 1 hit.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]

SMART

SM00852. MoCF_biosynth. 1 hit.
[Graphical view]

SUPFAM

SSF53218. MoCF_biosynth. 1 hit.
SSF63867. MoeA_C. 1 hit.
SSF63882. MoeA_N. 1 hit.

TIGRFAMs

TIGR00177. Molyb_syn. 1 hit.

PROSITE

PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MOEA_ECOLI

Accession

Primary (citable) accession number: P12281

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	January 25, 2012
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program